Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment.

Détails

ID Serval
serval:BIB_2132D45084C0
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment.
Périodique
Nature Structural and Molecular Biology
Auteur(s)
Honigmann A., van den Bogaart G., Iraheta E., Risselada H.J., Milovanovic D., Mueller V., Müllar S., Diederichsen U., Fasshauer D., Grubmüller H., Hell S.W., Eggeling C., Kühnel K., Jahn R.
ISSN
1545-9985 (Electronic)
ISSN-L
1545-9985
Statut éditorial
Publié
Date de publication
2013
Peer-reviewed
Oui
Volume
20
Numéro
6
Pages
679-686
Langue
anglais
Résumé
Synaptic-vesicle exocytosis is mediated by the vesicular Ca(2+) sensor synaptotagmin-1. Synaptotagmin-1 interacts with the SNARE protein syntaxin-1A and acidic phospholipids such as phosphatidylinositol 4,5-bisphosphate (PIP2). However, it is unclear how these interactions contribute to triggering membrane fusion. Using PC12 cells from Rattus norvegicus and artificial supported bilayers, we show that synaptotagmin-1 interacts with the polybasic linker region of syntaxin-1A independent of Ca(2+) through PIP2. This interaction allows both Ca(2+)-binding sites of synaptotagmin-1 to bind to phosphatidylserine in the vesicle membrane upon Ca(2+) triggering. We determined the crystal structure of the C2B domain of synaptotagmin-1 bound to phosphoserine, allowing development of a high-resolution model of synaptotagmin bridging two different membranes. Our results suggest that PIP2 clusters organized by syntaxin-1 act as molecular beacons for vesicle docking, with the subsequent Ca(2+) influx bringing the vesicle membrane close enough for membrane fusion.
Pubmed
Web of science
Création de la notice
23/07/2013 13:27
Dernière modification de la notice
20/08/2019 12:57
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